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:::::Collagen fibrils, sectioned longitudinally and transversely  (from Deane, Massey thesis, 1991).
 
:::::Collagen fibrils, sectioned longitudinally and transversely  (from Deane, Massey thesis, 1991).
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'''Collagen matures with age'''
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Stable aggregations of collagen molecules to form fibrils are achieved by cross-linking of the molecules.  These give collagen both strength and elasticity.  In newly formed collagen, the cross-links are relatively few, but with age, there is a significant increase in the number and the stability of the cross-links.  This has two significant effects.  Excessive stress on immature collagen contributes to tendon and ligament disease in young animals; the training of horses especially must take the aging of collagen into account.  Also, variations in collagen cross-links cause the toughness associated with different cuts of meat, and with the increase in toughness in meat from older animals.
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[[File:QMSection2.10.png|thumb|'''Fig. 2.10 Collagen cross-links''']]
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:::::'''Fig. 2.10   Collagen cross-links'''
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:::::Crosslinks in immature connective tissue pass between collagen molecules within a fibril (a).  The molecules are linked head to tail to form an infinite polymer. 
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::::In a mature collagen fibre, (b), the crosslinks pass between the fibrils to link them in register. 
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:::::(Adapted from Bailey, 1988).
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[[File:QMSection2.11.png|thumb|'''Fig. 11 Tensile stress in collagen''']]
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::::'''Fig. 11 Tensile stress in collagen'''
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::::The stress–strain relationship in a bundle of collagen fibres, at a low rate of strain. 
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::::Phase I:  Rapid elongation as the "crimp" in the collagen fibres is eliminated.  This part of the curve is smaller at the high strain rates likely to occur in vivo. 
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::::Phase II:  Stress is proportional to strain.  This elastic phase of collagen is the phase most useful in vivo. 
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::::Phase III:  Breakdown of the crystalline components of the collagen fibres.  Deformation takes place with progressively less stress.
     

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